Arginine methylation of the cellular nucleic acid binding protein does not affect its subcellular localization but impedes RNA binding

FEBS Lett. 2014 May 2;588(9):1542-8. doi: 10.1016/j.febslet.2014.03.052. Epub 2014 Apr 12.

Abstract

Cellular nucleic acid binding protein (CNBP) contains seven zinc finger (ZF) repeats and an arginine and glycine (RG) rich sequence between the first and the second ZF. CNBP interacts with protein arginine methyltransferase PRMT1. Full-length but not RG-deleted or mutated CNBP can be methylated. Treatment with a methylation inhibitor AdOx reduced CNBP methylation, but did not affect the concentrated nuclear localization of CNBP. Nevertheless, arginine methylation of CNBP appeared to interfere with its RNA binding activity. Our findings show that arginine methylation of CNBP in the RG motif did not change the subcellular localization, but regulated its RNA binding activity.

Keywords: CNBP; Protein arginine methylation; RNA binding.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Arginine / chemistry
  • Arginine / metabolism*
  • Binding, Competitive
  • HeLa Cells
  • Humans
  • Methylation
  • Protein Binding
  • Protein Processing, Post-Translational*
  • Protein Transport
  • Protein-Arginine N-Methyltransferases / metabolism
  • RNA / chemistry
  • RNA-Binding Proteins / chemistry
  • RNA-Binding Proteins / metabolism*
  • Repressor Proteins / metabolism

Substances

  • CNBP protein, human
  • RNA-Binding Proteins
  • Repressor Proteins
  • RNA
  • Arginine
  • PRMT1 protein, human
  • Protein-Arginine N-Methyltransferases